ID   ASE1_SCHPO              Reviewed;         731 AA.
AC   Q9HDY1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Anaphase spindle elongation protein 1;
GN   Name=ase1; ORFNames=SPAPB1A10.09;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15647375; DOI=10.1091/mbc.e04-10-0859;
RA   Yamashita A., Sato M., Fujita A., Yamamoto M., Toda T.;
RT   "The roles of fission yeast ase1 in mitotic cell division, meiotic nuclear
RT   oscillation, and cytokinesis checkpoint signaling.";
RL   Mol. Biol. Cell 16:1378-1395(2005).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KLP9.
RX   PubMed=19686686; DOI=10.1016/j.devcel.2009.06.012;
RA   Fu C., Ward J.J., Loiodice I., Velve-Casquillas G., Nedelec F.J.,
RA   Tran P.T.;
RT   "Phospho-regulated interaction between kinesin-6 Klp9p and microtubule
RT   bundler Ase1p promotes spindle elongation.";
RL   Dev. Cell 17:257-267(2009).
CC   -!- FUNCTION: Required for anaphase spindle elongation and microtubule
CC       bundling in both interphase and mitosis. Has a role in spatial and
CC       temporal regulation of septation and cytokinesis and ensures equal
CC       partition of segregating sister chromatids. Ensures correct midzone
CC       positioning of protein kinase ark1. Acts as a regulatory component at
CC       cytokinesis checkpoint where it inhibits nuclear division when
CC       actomyosin ring formation is impaired. {ECO:0000269|PubMed:15647375,
CC       ECO:0000269|PubMed:19686686}.
CC   -!- SUBUNIT: Interacts with klp9. {ECO:0000269|PubMed:19686686}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC       spindle. Note=Localizes to microtubule overlapping zones during
CC       interphase and spindle midzone during anaphase.
CC   -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAC21482.1; -; Genomic_DNA.
DR   RefSeq; NP_593523.1; NM_001018957.2.
DR   AlphaFoldDB; Q9HDY1; -.
DR   SMR; Q9HDY1; -.
DR   BioGRID; 279794; 200.
DR   STRING; 4896.SPAPB1A10.09.1; -.
DR   iPTMnet; Q9HDY1; -.
DR   MaxQB; Q9HDY1; -.
DR   PaxDb; Q9HDY1; -.
DR   PRIDE; Q9HDY1; -.
DR   EnsemblFungi; SPAPB1A10.09.1; SPAPB1A10.09.1:pep; SPAPB1A10.09.
DR   GeneID; 2543372; -.
DR   KEGG; spo:SPAPB1A10.09; -.
DR   PomBase; SPAPB1A10.09; ase1.
DR   VEuPathDB; FungiDB:SPAPB1A10.09; -.
DR   eggNOG; KOG4302; Eukaryota.
DR   HOGENOM; CLU_379049_0_0_1; -.
DR   InParanoid; Q9HDY1; -.
DR   OMA; YYREAPE; -.
DR   PhylomeDB; Q9HDY1; -.
DR   PRO; PR:Q9HDY1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0055028; C:cortical microtubule; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR   GO; GO:0000923; C:equatorial microtubule organizing center; IDA:PomBase.
DR   GO; GO:1990385; C:meiotic spindle midzone; IMP:PomBase.
DR   GO; GO:0015630; C:microtubule cytoskeleton; HDA:PomBase.
DR   GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR   GO; GO:1990498; C:mitotic spindle microtubule; IDA:PomBase.
DR   GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR   GO; GO:0097431; C:mitotic spindle pole; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IC:PomBase.
DR   GO; GO:0005819; C:spindle; IBA:GO_Central.
DR   GO; GO:0099070; C:static microtubule bundle; IDA:PomBase.
DR   GO; GO:0008017; F:microtubule binding; IDA:PomBase.
DR   GO; GO:0099609; F:microtubule lateral binding; IDA:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IMP:PomBase.
DR   GO; GO:0051232; P:meiotic spindle elongation; EXP:PomBase.
DR   GO; GO:0140642; P:meiotic spindle formation (spindle phase two); IMP:PomBase.
DR   GO; GO:1903563; P:microtubule bundle formation involved in horsetail-astral microtubule organization; IMP:PomBase.
DR   GO; GO:1903562; P:microtubule bundle formation involved in mitotic spindle midzone assembly; IDA:PomBase.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IGI:PomBase.
DR   GO; GO:0140515; P:mitotic nuclear bridge organization; IMP:PomBase.
DR   GO; GO:0000022; P:mitotic spindle elongation; IMP:PomBase.
DR   GO; GO:0061804; P:mitotic spindle formation (spindle phase one); IMP:PomBase.
DR   GO; GO:0140641; P:mitotic spindle formation (spindle phase two); IMP:PomBase.
DR   GO; GO:0051256; P:mitotic spindle midzone assembly; IGI:PomBase.
DR   GO; GO:0062168; P:negative regulation of plus-end directed microtubule sliding; IDA:PomBase.
DR   InterPro; IPR007145; MAP65_Ase1_PRC1.
DR   PANTHER; PTHR19321; PTHR19321; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..731
FT                   /note="Anaphase spindle elongation protein 1"
FT                   /id="PRO_0000363368"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   731 AA;  83173 MW;  249C3DF49E51912B CRC64;
     MQTVMMDDIQ STDSIAEKDN HSNNESNFTW KAFREQVEKH FSKIERLHQV LGTDGDNSSL
     FELFTTAMNA QLHEMEQCQK KLEDDCQQRI DSIRFLVSSL KLTDDTSSLK IESPLIQCLN
     RLSMVEGQYM AQYDQKLSTI KEMYHKLESY CNRLGSPFVL PDFENSFLSD VSDAFTESLR
     GRINEAEKEI DARLEVINSF EEEILGLWSE LGVEPADVPQ YEQLLESHTN RPNDVYVTQE
     LIDQLCKQKE VFSAEKEKRS DHLKSIQSEV SNLWNKLQVS PNEQSQFGDS SNINQENISL
     WETELEKLHQ LKKEHLPIFL EDCRQQILQL WDSLFYSEEQ RKSFTPMYED IITEQVLTAH
     ENYIKQLEAE VSANKSFLSL INRYASLIEG KKELEASSND ASRLTQRGRR DPGLLLREEK
     IRKRLSRELP KVQSLLIPEI TAWEERNGRT FLFYDEPLLK ICQEATQPKS LYRSASAAAN
     RPKTATTTDS VNRTPSQRGR VAVPSTPSVR SASRAMTSPR TPLPRVKNTQ NPSRSISAEP
     PSATSTANRR HPTANRIDIN ARLNSASRSR SANMIRQGAN GSDSNMSSSP VSGNSNTPFN
     KFPNSVSRNT HFESKSPHPN YSRTPHETYS KASSKNVPLS PPKQRVVNEH ALNIMSEKLQ
     RTNLKEQTPE MDIENSSQNL PFSPMKISPI RASPVKTIPS SPSPTTNIFS APLNNITNCT
     PMEDEWGEEG F